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Cited by 392

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease.

Open access
Fuller, R S, Brake, A, Thorner, J·1989·Proceedings of the National Academy of Sciences

Abstract

The KEX2-encoded endoprotease was overproduced in yeast several hundred-fold and further purified to achieve a 10,000-fold enrichment in specific activity. The enzyme was (i) membrane-bound, but solubilized by detergents; (ii) able to cleave peptide substrates at both Lys-Arg and Arg-Arg sites; (iii) inhibited by EDTA and EGTA (but not o-phenanthroline), but fully reactivated by Ca2+; (iv) unaffected by 5-10 mM phenylmethylsulfonyl fluoride, N alpha-(ptosyl)lysine chloromethyl ketone, or L-1-tosylamido-2-phenylethyl chloromethyl ketone, but inactivated by 1-2 microM Ala-Lys-Arg-chloromethyl ketone; (v) labeled specifically by 125I-labeled Tyr-Ala-Lys-Arg-chloromethyl ketone; and (vi) resistant to trans-epoxysuccinate compounds (which inactivate thiol proteases), but inactivated by diisopropyl fluorophosphate (a diagnostic serine protease inhibitor). Mutant enzyme molecules lacking as many as 200 C-terminal residues still retained Ca2+-dependent protease activity and were labeled by 125I-labeled Tyr-Ala-Lys-Arg-chloromethyl ketone.

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Metadata

Authors
Fuller, R. S., Brake, A., & Thorner, J.
Venue
Proceedings of the National Academy of Sciences
Published
1989-03
Volume
86
Issue
5
Pages
1434-1438
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2093508320
Cited by
392
References
1
FWCI
11.16
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. https://app.cochat.ai/papers/10.1073/pnas.86.5.1434
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Fuller, R. S., Brake, A., & Thorner, J. (1989). Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.5.1434

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